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Control of Rad52 recombination activity by double-strand break-induced SUMO modification.
Nat Cell Biol. 2006 Nov; 8(11):1284-90.NC

Abstract

Homologous recombination is essential for genetic exchange, meiosis and error-free repair of double-strand breaks. Central to this process is Rad52, a conserved homo-oligomeric ring-shaped protein, which mediates the exchange of the early recombination factor RPA by Rad51 and promotes strand annealing. Here, we report that Rad52 of Saccharomyces cerevisiae is modified by the ubiquitin-like protein SUMO, primarily at two sites that flank the conserved Rad52 domain. Sumoylation is induced on DNA damage and triggered by Mre11-Rad50-Xrs2 (MRX) complex-governed double-strand breaks (DSBs). Although sumoylation-defective Rad52 is largely recombination proficient, mutant analysis revealed that the SUMO modification sustains Rad52 activity and concomitantly shelters the protein from accelerated proteasomal degradation. Furthermore, our data indicate that sumoylation becomes particularly relevant for those Rad52 molecules that are engaged in recombination.

Authors+Show Affiliations

Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17013376

Citation

Sacher, Meik, et al. "Control of Rad52 Recombination Activity By Double-strand Break-induced SUMO Modification." Nature Cell Biology, vol. 8, no. 11, 2006, pp. 1284-90.
Sacher M, Pfander B, Hoege C, et al. Control of Rad52 recombination activity by double-strand break-induced SUMO modification. Nat Cell Biol. 2006;8(11):1284-90.
Sacher, M., Pfander, B., Hoege, C., & Jentsch, S. (2006). Control of Rad52 recombination activity by double-strand break-induced SUMO modification. Nature Cell Biology, 8(11), 1284-90.
Sacher M, et al. Control of Rad52 Recombination Activity By Double-strand Break-induced SUMO Modification. Nat Cell Biol. 2006;8(11):1284-90. PubMed PMID: 17013376.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Control of Rad52 recombination activity by double-strand break-induced SUMO modification. AU - Sacher,Meik, AU - Pfander,Boris, AU - Hoege,Carsten, AU - Jentsch,Stefan, Y1 - 2006/10/01/ PY - 2006/02/23/received PY - 2006/08/02/accepted PY - 2006/10/3/pubmed PY - 2006/12/13/medline PY - 2006/10/3/entrez SP - 1284 EP - 90 JF - Nature cell biology JO - Nat Cell Biol VL - 8 IS - 11 N2 - Homologous recombination is essential for genetic exchange, meiosis and error-free repair of double-strand breaks. Central to this process is Rad52, a conserved homo-oligomeric ring-shaped protein, which mediates the exchange of the early recombination factor RPA by Rad51 and promotes strand annealing. Here, we report that Rad52 of Saccharomyces cerevisiae is modified by the ubiquitin-like protein SUMO, primarily at two sites that flank the conserved Rad52 domain. Sumoylation is induced on DNA damage and triggered by Mre11-Rad50-Xrs2 (MRX) complex-governed double-strand breaks (DSBs). Although sumoylation-defective Rad52 is largely recombination proficient, mutant analysis revealed that the SUMO modification sustains Rad52 activity and concomitantly shelters the protein from accelerated proteasomal degradation. Furthermore, our data indicate that sumoylation becomes particularly relevant for those Rad52 molecules that are engaged in recombination. SN - 1465-7392 UR - https://www.unboundmedicine.com/medline/citation/17013376/Control_of_Rad52_recombination_activity_by_double_strand_break_induced_SUMO_modification_ L2 - https://doi.org/10.1038/ncb1488 DB - PRIME DP - Unbound Medicine ER -